data_25620 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N chemical shift assignments for the ground state-like fold of the single mutant G89A of dimeric KaiB from the Thermosynechococcus elongatus BP-1 cyanobacterial species ; _BMRB_accession_number 25620 _BMRB_flat_file_name bmr25620.str _Entry_type original _Submission_date 2015-05-16 _Accession_date 2015-05-16 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chang Yonggang . . 2 Cohen Susan . . 3 Phong Connie . . 4 Myers William . . 5 Kim Yong-Ick . . 6 Tseng Roger . . 7 Lin Jenny . . 8 Zhang Li . . 9 Boyd Joseph . . 10 Lee Yvonne . . 11 Kang Shannon . . 12 Lee David . . 13 Li Sheng . . 14 Britt R. . . 15 Rust Michael . . 16 Golden Susan . . 17 LiWang Andy . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 61 "13C chemical shifts" 199 "15N chemical shifts" 61 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-08-24 update BMRB 'update entry citation' 2015-07-14 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 25616 'KaiB dimer' 25617 'dimeric KaiB bound to CI' 25618 N-SasA 25619 'N-SasA bound to CI' 25621 'D91R single mutant of dimeric KaiB' 25622 'D91R single mutant of dimeric KaiB (thioredoxin-like fold)' 25623 'G89A,D91R double mutant of dimeric KaiB' 25624 'G89A,D91R double mutant of KaiB' 25625 'G89A,D91R double mutant of KaiB bound to CI' 25626 'G88A,D90R double mutant of KaiB' stop_ _Original_release_date 2015-07-14 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; A Protein Fold Switch Joins the Circadian Oscillator to Clock Output in Cyanobacteria ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26113641 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chang Yonggang . . 2 Cohen Susan . . 3 Phong Connie . . 4 Myers William . . 5 Kim Yong-Ick . . 6 Tseng Roger . . 7 Lin Jenny . . 8 Zhang Li . . 9 Boyd Joseph . . 10 Lee Yvonne . . 11 Kang Shannon . . 12 Lee David . . 13 Li Sheng . . 14 Britt R. . . 15 Rust Michael . . 16 Golden Susan . . 17 LiWang Andy . . stop_ _Journal_abbreviation Science _Journal_volume 349 _Journal_issue 6245 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 324 _Page_last 328 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'G89A single mutant of dimeric KaiB' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'KaiB, chain 1' $FTBN94YYG89AF_gs 'KaiB, chain 2' $FTBN94YYG89AF_gs stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_FTBN94YYG89AF_gs _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FTBN94YYG89AF_gs _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 110 _Mol_residue_sequence ; DYKDDDDKMAPLRKTAVLKL YVAGNTPNSVRALKTLNNIL EKEFKGVYALKVIDVLKNPQ LAEEDKILATPTLAKVLPPP VRRIIGDLSNREKVLIALDL LADYKDDDDK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ASP 2 2 TYR 3 3 LYS 4 4 ASP 5 5 ASP 6 6 ASP 7 7 ASP 8 8 LYS 9 9 MET 10 10 ALA 11 11 PRO 12 12 LEU 13 13 ARG 14 14 LYS 15 15 THR 16 16 ALA 17 17 VAL 18 18 LEU 19 19 LYS 20 20 LEU 21 21 TYR 22 22 VAL 23 23 ALA 24 24 GLY 25 25 ASN 26 26 THR 27 27 PRO 28 28 ASN 29 29 SER 30 30 VAL 31 31 ARG 32 32 ALA 33 33 LEU 34 34 LYS 35 35 THR 36 36 LEU 37 37 ASN 38 38 ASN 39 39 ILE 40 40 LEU 41 41 GLU 42 42 LYS 43 43 GLU 44 44 PHE 45 45 LYS 46 46 GLY 47 47 VAL 48 48 TYR 49 49 ALA 50 50 LEU 51 51 LYS 52 52 VAL 53 53 ILE 54 54 ASP 55 55 VAL 56 56 LEU 57 57 LYS 58 58 ASN 59 59 PRO 60 60 GLN 61 61 LEU 62 62 ALA 63 63 GLU 64 64 GLU 65 65 ASP 66 66 LYS 67 67 ILE 68 68 LEU 69 69 ALA 70 70 THR 71 71 PRO 72 72 THR 73 73 LEU 74 74 ALA 75 75 LYS 76 76 VAL 77 77 LEU 78 78 PRO 79 79 PRO 80 80 PRO 81 81 VAL 82 82 ARG 83 83 ARG 84 84 ILE 85 85 ILE 86 86 GLY 87 87 ASP 88 88 LEU 89 89 SER 90 90 ASN 91 91 ARG 92 92 GLU 93 93 LYS 94 94 VAL 95 95 LEU 96 96 ILE 97 97 ALA 98 98 LEU 99 99 ASP 100 100 LEU 101 101 LEU 102 102 ALA 103 103 ASP 104 104 TYR 105 105 LYS 106 106 ASP 107 107 ASP 108 108 ASP 109 109 ASP 110 110 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $FTBN94YYG89AF_gs cyanobacteria 146786 Bacteria . Thermosynechococcus elongatus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $FTBN94YYG89AF_gs 'recombinant technology' . Escherichia coli . pET-28b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; Sample: [N15,C13]-FLAG-TeKaiB-1-94-Y8A-Y94A-G89A-FLAG (1760 uM); Bufffer: 20 mM Tris, 100 mM NaCl, pH 7.0, 10 uM DSS, 0.02% NaN3, 95%H2O/5%D2O; Volume: 320 uL; Tube: shaped ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FTBN94YYG89AF_gs 1760 uM '[U-99% 13C; U-98% 15N]' Tris 20 mM 'natural abundance' NaCl 100 mM 'natural abundance' DSS 10 uM 'natural abundance' NaNa3 0.02 % 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_Mars _Saveframe_category software _Name Mars _Version . loop_ _Vendor _Address _Electronic_address 'Young-Sang Jung and Markus Zweckstetter' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'Bruker 600 MHz AVANCE III spectrometer equipped with a TCI cryoprobe and z-axis pulsed-field gradient capability' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 . M pH 7.0 . pH pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl carbons' MHz 601.1299434 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D HN(CO)CACB' '3D HNCA' '3D HN(CO)CA' '3D HN(CA)CO' '3D HNCO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'KaiB, chain 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 15 15 THR C C 173.200 . 1 2 15 15 THR CA C 62.870 . 1 3 15 15 THR CB C 70.340 . 1 4 16 16 ALA H H 8.085 . 1 5 16 16 ALA C C 176.400 . 1 6 16 16 ALA CA C 51.340 . 1 7 16 16 ALA CB C 20.840 . 1 8 16 16 ALA N N 127.900 . 1 9 17 17 VAL H H 8.723 . 1 10 17 17 VAL C C 174.200 . 1 11 17 17 VAL CA C 61.680 . 1 12 17 17 VAL CB C 33.880 . 1 13 17 17 VAL N N 121.500 . 1 14 18 18 LEU H H 9.007 . 1 15 18 18 LEU C C 173.300 . 1 16 18 18 LEU CA C 53.390 . 1 17 18 18 LEU CB C 43.100 . 1 18 18 18 LEU N N 130.500 . 1 19 19 19 LYS H H 8.920 . 1 20 19 19 LYS C C 174.500 . 1 21 19 19 LYS CA C 54.660 . 1 22 19 19 LYS CB C 34.570 . 1 23 19 19 LYS N N 126.300 . 1 24 20 20 LEU H H 8.685 . 1 25 20 20 LEU C C 174.200 . 1 26 20 20 LEU CA C 53.730 . 1 27 20 20 LEU CB C 43.290 . 1 28 20 20 LEU N N 123.400 . 1 29 21 21 TYR H H 8.684 . 1 30 21 21 TYR C C 175.400 . 1 31 21 21 TYR CA C 56.620 . 1 32 21 21 TYR CB C 37.260 . 1 33 21 21 TYR N N 122.500 . 1 34 22 22 VAL H H 9.244 . 1 35 22 22 VAL C C 174.500 . 1 36 22 22 VAL CA C 58.600 . 1 37 22 22 VAL CB C 34.920 . 1 38 22 22 VAL N N 119.000 . 1 39 23 23 ALA H H 9.354 . 1 40 23 23 ALA C C 175.600 . 1 41 23 23 ALA CA C 50.120 . 1 42 23 23 ALA CB C 18.230 . 1 43 23 23 ALA N N 128.600 . 1 44 24 24 GLY H H 8.054 . 1 45 24 24 GLY C C 171.500 . 1 46 24 24 GLY CA C 44.780 . 1 47 24 24 GLY N N 110.700 . 1 48 25 25 ASN H H 8.041 . 1 49 25 25 ASN C C 174.000 . 1 50 25 25 ASN CA C 52.520 . 1 51 25 25 ASN CB C 42.570 . 1 52 25 25 ASN N N 112.900 . 1 53 26 26 THR H H 9.100 . 1 54 26 26 THR CA C 58.740 . 1 55 26 26 THR CB C 69.740 . 1 56 26 26 THR N N 113.700 . 1 57 27 27 PRO C C 179.900 . 1 58 27 27 PRO CA C 66.280 . 1 59 27 27 PRO CB C 31.650 . 1 60 28 28 ASN H H 8.544 . 1 61 28 28 ASN C C 178.800 . 1 62 28 28 ASN CA C 55.160 . 1 63 28 28 ASN CB C 37.730 . 1 64 28 28 ASN N N 113.000 . 1 65 29 29 SER H H 8.979 . 1 66 29 29 SER C C 175.900 . 1 67 29 29 SER CA C 62.690 . 1 68 29 29 SER N N 123.400 . 1 69 30 30 VAL H H 8.395 . 1 70 30 30 VAL C C 179.400 . 1 71 30 30 VAL CA C 66.920 . 1 72 30 30 VAL CB C 31.690 . 1 73 30 30 VAL N N 124.700 . 1 74 31 31 ARG H H 7.337 . 1 75 31 31 ARG C C 178.900 . 1 76 31 31 ARG CA C 59.650 . 1 77 31 31 ARG CB C 30.340 . 1 78 31 31 ARG N N 119.400 . 1 79 32 32 ALA C C 179.800 . 1 80 32 32 ALA CA C 55.200 . 1 81 32 32 ALA CB C 18.420 . 1 82 33 33 LEU H H 8.493 . 1 83 33 33 LEU C C 179.800 . 1 84 33 33 LEU CA C 58.060 . 1 85 33 33 LEU CB C 41.700 . 1 86 33 33 LEU N N 118.400 . 1 87 34 34 LYS H H 7.854 . 1 88 34 34 LYS C C 179.400 . 1 89 34 34 LYS CA C 59.930 . 1 90 34 34 LYS CB C 31.870 . 1 91 34 34 LYS N N 122.000 . 1 92 35 35 THR H H 8.321 . 1 93 35 35 THR C C 176.300 . 1 94 35 35 THR CA C 66.950 . 1 95 35 35 THR CB C 68.420 . 1 96 35 35 THR N N 118.600 . 1 97 36 36 LEU H H 8.872 . 1 98 36 36 LEU C C 177.500 . 1 99 36 36 LEU CA C 58.240 . 1 100 36 36 LEU CB C 41.380 . 1 101 36 36 LEU N N 122.100 . 1 102 37 37 ASN H H 8.249 . 1 103 37 37 ASN C C 177.000 . 1 104 37 37 ASN CA C 57.620 . 1 105 37 37 ASN CB C 39.460 . 1 106 37 37 ASN N N 117.000 . 1 107 38 38 ASN H H 8.054 . 1 108 38 38 ASN C C 177.800 . 1 109 38 38 ASN CA C 56.620 . 1 110 38 38 ASN CB C 38.450 . 1 111 38 38 ASN N N 117.000 . 1 112 41 41 GLU CA C 59.030 . 1 113 41 41 GLU CB C 30.290 . 1 114 42 42 LYS H H 8.089 . 1 115 42 42 LYS C C 178.500 . 1 116 42 42 LYS CA C 58.140 . 1 117 42 42 LYS CB C 33.550 . 1 118 42 42 LYS N N 116.000 . 1 119 43 43 GLU H H 8.577 . 1 120 43 43 GLU C C 177.000 . 1 121 43 43 GLU CA C 57.520 . 1 122 43 43 GLU CB C 31.060 . 1 123 43 43 GLU N N 117.100 . 1 124 44 44 PHE H H 7.628 . 1 125 44 44 PHE C C 175.600 . 1 126 44 44 PHE CA C 56.870 . 1 127 44 44 PHE CB C 40.050 . 1 128 44 44 PHE N N 116.000 . 1 129 45 45 LYS H H 7.726 . 1 130 45 45 LYS C C 178.400 . 1 131 45 45 LYS CA C 58.740 . 1 132 45 45 LYS CB C 31.230 . 1 133 45 45 LYS N N 121.700 . 1 134 46 46 GLY H H 9.199 . 1 135 46 46 GLY C C 174.300 . 1 136 46 46 GLY CA C 45.790 . 1 137 46 46 GLY N N 113.500 . 1 138 47 47 VAL C C 175.900 . 1 139 47 47 VAL CA C 65.160 . 1 140 47 47 VAL CB C 32.890 . 1 141 48 48 TYR H H 7.901 . 1 142 48 48 TYR C C 174.900 . 1 143 48 48 TYR CA C 56.000 . 1 144 48 48 TYR CB C 43.240 . 1 145 48 48 TYR N N 114.800 . 1 146 49 49 ALA H H 8.639 . 1 147 49 49 ALA C C 175.200 . 1 148 49 49 ALA CA C 50.760 . 1 149 49 49 ALA CB C 21.400 . 1 150 49 49 ALA N N 124.400 . 1 151 50 50 LEU H H 8.779 . 1 152 50 50 LEU C C 176.300 . 1 153 50 50 LEU CA C 54.450 . 1 154 50 50 LEU CB C 44.720 . 1 155 50 50 LEU N N 123.400 . 1 156 51 51 LYS H H 8.954 . 1 157 51 51 LYS C C 173.500 . 1 158 51 51 LYS CA C 55.090 . 1 159 51 51 LYS CB C 35.660 . 1 160 51 51 LYS N N 127.800 . 1 161 52 52 VAL H H 8.655 . 1 162 52 52 VAL C C 175.300 . 1 163 52 52 VAL CA C 62.110 . 1 164 52 52 VAL CB C 33.120 . 1 165 52 52 VAL N N 125.400 . 1 166 53 53 ILE H H 9.291 . 1 167 53 53 ILE C C 173.900 . 1 168 53 53 ILE CA C 59.800 . 1 169 53 53 ILE CB C 39.400 . 1 170 53 53 ILE N N 131.100 . 1 171 54 54 ASP H H 8.698 . 1 172 54 54 ASP C C 178.300 . 1 173 54 54 ASP CA C 52.800 . 1 174 54 54 ASP CB C 41.080 . 1 175 54 54 ASP N N 127.100 . 1 176 55 55 VAL H H 9.185 . 1 177 55 55 VAL C C 177.000 . 1 178 55 55 VAL CA C 61.870 . 1 179 55 55 VAL CB C 31.150 . 1 180 55 55 VAL N N 121.000 . 1 181 56 56 LEU H H 8.749 . 1 182 56 56 LEU C C 179.100 . 1 183 56 56 LEU CA C 57.350 . 1 184 56 56 LEU CB C 41.280 . 1 185 56 56 LEU N N 122.400 . 1 186 57 57 LYS H H 7.648 . 1 187 57 57 LYS C C 176.600 . 1 188 57 57 LYS CA C 57.000 . 1 189 57 57 LYS CB C 33.240 . 1 190 57 57 LYS N N 117.200 . 1 191 58 58 ASN H H 7.602 . 1 192 58 58 ASN CA C 51.180 . 1 193 58 58 ASN CB C 39.720 . 1 194 58 58 ASN N N 114.700 . 1 195 59 59 PRO C C 178.400 . 1 196 59 59 PRO CA C 64.920 . 1 197 59 59 PRO CB C 31.690 . 1 198 60 60 GLN H H 8.656 . 1 199 60 60 GLN C C 176.400 . 1 200 60 60 GLN CA C 56.860 . 1 201 60 60 GLN CB C 27.700 . 1 202 60 60 GLN N N 117.800 . 1 203 61 61 LEU H H 7.794 . 1 204 61 61 LEU C C 177.100 . 1 205 61 61 LEU CA C 55.380 . 1 206 61 61 LEU CB C 42.120 . 1 207 61 61 LEU N N 119.100 . 1 208 62 62 ALA H H 7.501 . 1 209 62 62 ALA C C 175.600 . 1 210 62 62 ALA CA C 51.330 . 1 211 62 62 ALA CB C 18.070 . 1 212 62 62 ALA N N 122.000 . 1 213 63 63 GLU H H 7.768 . 1 214 63 63 GLU C C 177.100 . 1 215 63 63 GLU CA C 56.380 . 1 216 63 63 GLU CB C 30.990 . 1 217 63 63 GLU N N 121.500 . 1 218 64 64 GLU H H 8.846 . 1 219 64 64 GLU C C 177.600 . 1 220 64 64 GLU CA C 59.680 . 1 221 64 64 GLU CB C 29.720 . 1 222 64 64 GLU N N 123.600 . 1 223 65 65 ASP H H 8.810 . 1 224 65 65 ASP CA C 56.710 . 1 225 65 65 ASP CB C 39.730 . 1 226 65 65 ASP N N 117.100 . 1 227 66 66 LYS H H 7.450 . 1 228 66 66 LYS CA C 57.310 . 1 229 66 66 LYS CB C 31.980 . 1 230 66 66 LYS N N 118.900 . 1 231 71 71 PRO C C 178.800 . 1 232 71 71 PRO CA C 65.580 . 1 233 71 71 PRO CB C 31.230 . 1 234 72 72 THR H H 7.485 . 1 235 72 72 THR CA C 65.470 . 1 236 72 72 THR CB C 68.810 . 1 237 72 72 THR N N 113.000 . 1 238 73 73 LEU C C 178.400 . 1 239 73 73 LEU CA C 57.000 . 1 240 74 74 ALA H H 8.321 . 1 241 74 74 ALA C C 178.500 . 1 242 74 74 ALA CA C 54.610 . 1 243 74 74 ALA CB C 17.930 . 1 244 74 74 ALA N N 118.200 . 1 245 75 75 LYS H H 7.053 . 1 246 75 75 LYS C C 177.600 . 1 247 75 75 LYS CA C 58.420 . 1 248 75 75 LYS CB C 32.880 . 1 249 75 75 LYS N N 111.300 . 1 250 76 76 VAL H H 7.400 . 1 251 76 76 VAL C C 176.600 . 1 252 76 76 VAL CA C 61.860 . 1 253 76 76 VAL CB C 31.660 . 1 254 76 76 VAL N N 111.800 . 1 255 77 77 LEU H H 7.241 . 1 256 77 77 LEU C C 173.400 . 1 257 77 77 LEU CA C 52.710 . 1 258 77 77 LEU CB C 40.550 . 1 259 77 77 LEU N N 121.900 . 1 260 85 85 ILE C C 178.400 . 1 261 85 85 ILE CA C 64.220 . 1 262 85 85 ILE CB C 36.190 . 1 263 86 86 GLY H H 8.373 . 1 264 86 86 GLY C C 176.000 . 1 265 86 86 GLY CA C 47.280 . 1 266 86 86 GLY N N 108.300 . 1 267 87 87 ASP H H 7.920 . 1 268 87 87 ASP C C 180.000 . 1 269 87 87 ASP CA C 57.880 . 1 270 87 87 ASP CB C 40.230 . 1 271 87 87 ASP N N 123.800 . 1 272 88 88 LEU H H 8.568 . 1 273 88 88 LEU C C 178.000 . 1 274 88 88 LEU CA C 57.840 . 1 275 88 88 LEU CB C 43.310 . 1 276 88 88 LEU N N 119.900 . 1 277 89 89 SER H H 8.329 . 1 278 89 89 SER C C 175.400 . 1 279 89 89 SER CA C 60.700 . 1 280 89 89 SER CB C 63.870 . 1 281 89 89 SER N N 113.700 . 1 282 90 90 ASN H H 8.776 . 1 283 90 90 ASN C C 175.700 . 1 284 90 90 ASN CA C 55.460 . 1 285 90 90 ASN CB C 39.850 . 1 286 90 90 ASN N N 116.400 . 1 287 91 91 ARG H H 7.948 . 1 288 91 91 ARG C C 177.200 . 1 289 91 91 ARG CA C 58.360 . 1 290 91 91 ARG CB C 30.760 . 1 291 91 91 ARG N N 118.600 . 1 292 92 92 GLU H H 8.301 . 1 293 92 92 GLU C C 175.800 . 1 294 92 92 GLU CA C 56.240 . 1 295 92 92 GLU CB C 30.090 . 1 296 92 92 GLU N N 114.400 . 1 297 93 93 LYS H H 6.738 . 1 298 93 93 LYS C C 175.800 . 1 299 93 93 LYS CA C 57.400 . 1 300 93 93 LYS CB C 29.160 . 1 301 93 93 LYS N N 109.900 . 1 302 94 94 VAL H H 7.527 . 1 303 94 94 VAL C C 175.500 . 1 304 94 94 VAL CA C 61.020 . 1 305 94 94 VAL CB C 33.300 . 1 306 94 94 VAL N N 107.000 . 1 307 95 95 LEU H H 7.215 . 1 308 95 95 LEU C C 175.200 . 1 309 95 95 LEU CA C 55.300 . 1 310 95 95 LEU CB C 43.270 . 1 311 95 95 LEU N N 121.800 . 1 312 96 96 ILE H H 9.227 . 1 313 96 96 ILE C C 175.700 . 1 314 96 96 ILE CA C 60.500 . 1 315 96 96 ILE CB C 38.240 . 1 316 96 96 ILE N N 128.700 . 1 317 97 97 ALA H H 7.912 . 1 318 97 97 ALA C C 174.000 . 1 319 97 97 ALA CA C 51.080 . 1 320 97 97 ALA CB C 22.120 . 1 321 97 97 ALA N N 116.900 . 1 stop_ save_